scholarly journals Investigation into the distribution and properties of histones and other basic proteins in bacteria

1966 ◽  
Vol 101 (3) ◽  
pp. 665-673 ◽  
Author(s):  
JL Leaver ◽  
HJ Cruft
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Starch Gel Electrophoresis ◽  
Basic Proteins ◽  
E Coli ◽  
Extraction And Purification ◽  
Starch Gel ◽  
Micro Organisms

1. Methods have been developed for the extraction and purification of bacterial basic proteins. These proteins were initially examined by a micro-method of starch-gel electrophoresis and were then characterized more fully. 2. Although it was found that most of the DNA in both Bacillus megaterium and Escherichia coli must be free from combination with basic protein, there was some evidence that a small portion might be in the form of a typical nucleohistone complex. 3. The ribosomes of both B. megaterium and E. coli were shown to contain approximately 2% of basic protein. On the basis of ultraviolet-absorption curves, partial amino acid analyses and their behaviour on electrophoresis in polyacrylamide gels, it was concluded that some of these ribosomal basic proteins may be extremely similar to typical histones. 4. These results are discussed in relation to those of other authors, and the possible functions of basic proteins present in micro-organisms are considered with reference to those that have already been proposed for the histones of higher organisms.

scholarly journals Some relationships between R-factor and chromosomal β-lactamase in Gram-negative bacteria

1971 ◽  
Vol 123 (4) ◽  
pp. 507-512 ◽  
Author(s):  
J. W. Dale ◽  
J. T. Smith
Keyword(s):  
Gel Electrophoresis ◽  
Klebsiella Aerogenes ◽  
Gram Negative Bacteria ◽  
Starch Gel Electrophoresis ◽  
Gram Negative ◽  
E Coli ◽  
Molecular Weights ◽  
R Factor ◽  
Starch Gel ◽  
R Factors

1. The β-lactamases specified by Klebsiella aerogenes 418 and the R-factor R-7268 have been partially purified. 2. The molecular weights of the K. aerogenes strains 418 and 373, Aerobacter cloacae 53, R-7268 and R-TEM β-lactamases were all about 20000; that of the enzymes from Escherichia coli strains 419 and 214T was about 31000. 3. These enzymes were also compared by means of their Km values for benzylpenicillin and ampicillin, and their behaviour on starch-gel electrophoresis. 4. The β-lactamases specified by the two Klebsiella strains, the Aerobacter strain, and the R-factors R-TEM and R-7268 were found to comprise a broadly similar group. However, within this group, only two enzymes seemed to be identical, namely those specified by the two R-factors. The two E. coli strains produce identical β-lactamases which are very different from the ‘Klebsiella/Aerobacter-type’ enzymes.

The Separation of Insect Haemolymph Proteins

1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Homologous Proteins ◽  
Agar Gel ◽  
Diffusion Technique ◽  
Starch Gel ◽  
Rapid Characterization ◽  
Gel Diffusion

It has been suggested that information on the phylogenetic relationships of genera and species could be obtained by comparing the amino acid sequence in the homologous proteins of different species. This procedure is extremely difficult and time-consuming.However, a relatively rapid characterization of proteins can be obtained by analysing their mobilities with starch-gel electrophoresis and examination of antigenic diversity by the agar gel diffusion technique of Ouchterlony.

scholarly journals The Amino Acid Composition of Hemoglobin. III. A Qualitative Method for Identifying Abnormalities of the Polypeptide Chains of Hemoglobin

Blood ◽  
1964 ◽  
Vol 24 (6) ◽  
pp. 750-756 ◽  
Author(s):  
AMOZ I. CHERNOFF ◽  
NELSON M. PETTIT
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Gel Electrophoresis ◽  
Qualitative Method ◽  
Polypeptide Chain ◽  
Starch Gel Electrophoresis ◽  
Simple Method ◽  
Starch Gel ◽  
Barbital Buffer ◽  
Polypeptide Chains

Abstract A relatively simple method is described which permits the identification of abnormalities of either polypeptide chain of hemoglobin. The procedure is based on the dissociation of hemoglobin by 6 molar urea and starch-gel electrophoresis in a barbital buffer at pH 8.0.

scholarly journals The Fractionation of ?-Histones From Chicken Erythrocyte Nuclei

1964 ◽  
Vol 17 (4) ◽  
pp. 1001 ◽  
Author(s):  
JT Bellair ◽  
OM Mauritzen
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Chicken Erythrocyte ◽  
Exclusion Chromatography ◽  
Starch Gel

Crude IX-histone, obtained from the original histone complex by precipitation of the f3-and y-histones with ethanol, has been shown by starch-gel electrophoresis to contain 13 components. The fractionation of IX-histone by exclusion chromatography on Sephadex G-200 is reported. While none of these components have been obtained pure in the present study, considerable purification of components 2, 3, 4, 5, 8, 9, 10, and 11 has been achieved, and their amino acid composition leaves no doubt that o::-histones represent a muoh larger family of "lysine-rich" proteins than was hitherto supposed.

scholarly journals Ethanol Extraction of Basic Proteins From Ejaculated Human Spermatozoa

1979 ◽  
Vol 32 (5) ◽  
pp. 443 ◽  
Author(s):  
Peter French
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Banding Pattern ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ethanol Extraction ◽  
Basic Proteins ◽  
Unconventional Method

A method for the extraction of basic proteins from human ejaculated spermatozoa has been developed It relies on the previously unreported observation that such basic protein is soluble in a solution containing 60% (v/v) ethanol. This unconventional method yields a high percentage of arginine-rich basic protein which is then able to be characterized on the basis of its amino acid composition. This method also allows comparisons to be made between single ejaculates by the banding pattern each displays when subjected to polyacrylamide gel electrophoresis.

The tertiary phase of rennin action on αs- and β-caseins

1970 ◽  
Vol 37 (3) ◽  
pp. 437-444 ◽  
Author(s):  
A. M. El-Negoumy
Keyword(s):  
Amino Acid ◽  
Degradation Product ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Starch Gel Electrophoresis ◽  
Terminal Amino Acid ◽  
Starch Gel ◽  
Terminal Amino

SummaryCasein, whole αs-casein and β-casein were incubated for 3 and 14 h with crystalline rennin, at pH 6·60 and 36 °C, both in phosphate buffer and in milk dialysate. Products obtained from both systems, comprising 30–83% calciumsensitive (Cas) components, gave similar patterns on starch gel electrophoresis. Whole casein and whole αs-casein were not so soluble in milk dialysate as in phosphate buffer. No significant differences in composition were observed between the Cas and the calcium-insensitive (Ca1) products from the same source.The αs1-component of the Cas product from rennin-treated whole αs-casein had faster gel mobility in comparison to the αs1-component in the Cas product from untreated whole αs-casein. Also, αs1-casein yielded one faster-moving degradation product, while αs2,3,4 appeared unaltered after 14h. The Cas product of rennintreated β-casein also had faster mobility than untreated β-casein and yielded one faster degradation product and several minor ones of slower mobility. Arginine was the only N-terminal amino acid found in the Cas product of both rennin-treated and untreated αs - and β-caseins. The arginine content increased from 3·48 and 4·98 moles/105g to 5·12 and 6·38 moles/105g in the Cas products from rennin-treated β-and αs-caseins, respectively.

scholarly journals ENZYMES IN HOG KIDNEY HYDROLYZING AMINO ACID NAPHTHYLAMIDES

1966 ◽  
Vol 14 (4) ◽  
pp. 314-325 ◽  
Author(s):  
T. VANHA-PERTTULA ◽  
V. K. HOPSU ◽  
G. G. GLENNER
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Gel Electrophoresis ◽  
Metal Ion ◽  
Total Activity ◽  
Starch Gel Electrophoresis ◽  
Enzyme Preparations ◽  
Starch Gel ◽  
Hydrolysis Of ◽  
Hog Kidney

Hydrolysis of β-naphthylamides of a number of amino acids and dipeptides and of a number of di- and tripeptides by hog kidney homogenate and by fractions obtained by various fractionation procedures has been studied. The substrates were found to be split by a soluble, apparently sulfhydryl-dependent enzyme, and by a particle-bound, metal-activated enzyme. The former constituted only a small part of the total activity. The latter was subfractionated by starch gel electrophoresis into two fractions with identical characteristics. The soluble and particle-bound enzymes differed also in their substrate specificity. The latter enzyme was solubilized, partially purified, characterized by some modifier compounds and compared with enzyme preparations obtained by various fractionation procedures presented by other investigators. Thus enzyme showed ion-determined substrate specificity, i.e., hydrolysis of some of the amino acid naphthylamides was found to be activated by Co++ while the hydrolysis of others was inhibited by the same metal ion.

scholarly journals Horizontal Transfer of blaCMY-Bearing Plasmids among Clinical Escherichia coli and Klebsiella pneumoniae Isolates and Emergence of Cefepime-Hydrolyzing CMY-19

2006 ◽  
Vol 50 (2) ◽  
pp. 534-541 ◽  
Author(s):  
Jun-ichi Wachino ◽  
Hiroshi Kurokawa ◽  
Satowa Suzuki ◽  
Kunikazu Yamane ◽  
Naohiro Shibata ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Gel Electrophoresis ◽  
Southern Hybridization ◽  
Pulsed Field Gel Electrophoresis ◽  
The Other ◽  
Single Amino Acid ◽  
E Coli ◽  
Clonal Relatedness

ABSTRACT Nine Escherichia coli and 5 Klebsiella pneumoniae clinical isolates resistant to various cephalosporins and cephamycins were identified in a Japanese general hospital between 1995 and 1997. All nine E. coli isolates and one K. pneumoniae isolate carried bla CMY-9, while the other four K. pneumoniae isolates harbored a variant of bla CMY-9, namely, bla CMY-19. The pulsed-field gel electrophoresis patterns of the nine CMY-9-producing E. coli isolates were almost identical, suggesting their clonal relatedness, while those of the five K. pneumoniae isolates were divergent. Plasmid profiles, Southern hybridization, and conjugation assays revealed that the genes for the CMY-9 and the CMY-19 β-lactamases were located on very similar conjugative plasmids in E. coli and K. pneumoniae. The genetic environment of bla CMY-19 was identical to that of bla CMY-9. A single amino acid substitution, I292S, adjacent to the H-10 helix region was observed between CMY-9 and CMY-19. This substitution was suggested to be responsible for the expansion of the hydrolyzing activity against several broad-spectrum cephalosporins, and this finding was consistent with the kinetic parameters determined with purified enzymes. These findings suggest that the bla CMY-19 genes found in the four K. pneumoniae isolates might have originated from bla CMY-9 gene following a point mutation and dispersed among genetically different K. pneumoniae isolates via a large transferable plasmid.

scholarly journals The Amino Acid Composition of Hemoglobin. V. The Preparation of Purified Hemoglobin Fractions by Chromatography on Cellulose Exchangers and Their Identification by Starch Gel Electrophoresis Using Tris-Borate-EDTA Buffer

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 646-661 ◽  
Author(s):  
AMOZ I. CHERNOFF ◽  
NELSON PETTIT ◽  
JO NORTHROP
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Tris Borate Edta

Abstract The chromatographic separation of hemoglobin on two cellulose exchangers, CMC and DEAE, is discussed. Problems related to the use of these technics are described. In addition, our experience with the use of Tris-Borate-EDTA buffer (Smithies) for hemoglobin electrophoresis in starch gel is presented.

scholarly journals Studies on Reduced Wool

1964 ◽  
Vol 17 (4) ◽  
pp. 973 ◽  
Author(s):  
IJ O'donnell ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Single Component ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Wool Proteins

Starch-gel electrophoresis in buffers containing 8ror urea has been used to follow the fractionation of wool proteins extracted from reduced and carboxy-methylated wool. Fractionation on both DEAE-cellulose and Sephadex G-200 in the presence of buffers containing Sr.t: urea is possible but in neither case is a single component obtained. However, a combination of these two methods has enabled one of the major components to be isolated. The amino acid composition of this material is reported.

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